S100A14 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 124 amino acids (1-104 a.a.) and having a molecular mass of 13.8kDa. The S100A14 is purified by proprietary chromatographic techniques.
S100 Calcium Binding Protein A14 (S100A14) is a member of the S100 protein family, which is characterized by the presence of EF-hand calcium-binding motifs. This family of proteins is involved in a variety of intracellular and extracellular functions, including regulation of protein phosphorylation, enzyme activities, cell growth and differentiation, and the dynamics of cytoskeleton components .
The S100A14 gene is located on chromosome 1, within a cluster of other S100 genes . The gene encodes a protein that consists of 104 amino acids and has a molecular mass of approximately 13.8 kDa . The recombinant form of S100A14 is often produced in E. coli and includes a His-tag for purification purposes .
S100A14 plays a significant role in the regulation of cell survival and apoptosis by modulating the levels of the tumor suppressor protein p53 (TP53) . Depending on the cellular context, S100A14 can either promote cell proliferation or induce apoptosis . It also influences cell migration by regulating the levels of matrix metalloproteinase-2 (MMP2), which is under the transcriptional control of p53 .
Interestingly, despite being a member of the S100 family, S100A14 does not bind calcium . This unique characteristic differentiates it from other S100 proteins and suggests that its functions are mediated through different mechanisms.
S100A14 has been implicated in various cancers. Its expression levels are often found to be lower in cancerous tissues compared to normal tissues, suggesting a potential tumor suppressor function . For instance, reduced levels of S100A14 have been associated with metastasis in breast cancer . This makes S100A14 a potential biomarker for cancer diagnosis and prognosis.
Recombinant S100A14 is widely used in research to study its role in cancer biology and other cellular processes. It is also used to develop antibodies for diagnostic and therapeutic purposes . The recombinant protein is typically produced in mammalian or bacterial expression systems and purified using chromatographic techniques .